OpenAlex Citation Counts

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OpenAlex is a bibliographic catalogue of scientific papers, authors and institutions accessible in open access mode, named after the Library of Alexandria. It's citation coverage is excellent and I hope you will find utility in this listing of citing articles!

If you click the article title, you'll navigate to the article, as listed in CrossRef. If you click the Open Access links, you'll navigate to the "best Open Access location". Clicking the citation count will open this listing for that article. Lastly at the bottom of the page, you'll find basic pagination options.

Requested Article:

DNA activates the Nse2/Mms21 SUMO E3 ligase in the Smc5/6 complex
Nathalia Varejão, Eva Ibars, Jara Lascorz, et al.
The EMBO Journal (2018) Vol. 37, Iss. 12
Open Access | Times Cited: 48

Showing 1-25 of 48 citing articles:

The multi-functional Smc5/6 complex in genome protection and disease
Xiao Peng, Xiaolan Zhao
Nature Structural & Molecular Biology (2023) Vol. 30, Iss. 6, pp. 724-734
Open Access | Times Cited: 29

The SMC5/6 complex: folding chromosomes back into shape when genomes take a break
Shamayita Roy, Hemanta Adhikary, Damien D’Amours
Nucleic Acids Research (2024) Vol. 52, Iss. 5, pp. 2112-2129
Open Access | Times Cited: 9

Molecular mechanisms in SUMO conjugation
Nathalia Varejão, Jara Lascorz, Ying Li, et al.
Biochemical Society Transactions (2019) Vol. 48, Iss. 1, pp. 123-135
Closed Access | Times Cited: 70

Purified Smc5/6 Complex Exhibits DNA Substrate Recognition and Compaction
Pilar Gutiérrez-Escribano, Silvia Hormeño, Julene Madariaga-Marcos, et al.
Molecular Cell (2020) Vol. 80, Iss. 6, pp. 1039-1054.e6
Open Access | Times Cited: 68

Nse5/6 inhibits the Smc5/6 ATPase and modulates DNA substrate binding
Michael J. Taschner, J. Basquin, Barbara Steigenberger, et al.
The EMBO Journal (2021) Vol. 40, Iss. 15
Open Access | Times Cited: 44

KSHV RTA antagonizes SMC5/6 complex-induced viral chromatin compaction by hijacking the ubiquitin-proteasome system
Chunyan Han, Dun Zhang, Chenwu Gui, et al.
PLoS Pathogens (2022) Vol. 18, Iss. 8, pp. e1010744-e1010744
Open Access | Times Cited: 36

Combining Structural Aggregation Propensity and Stability Predictions To Redesign Protein Solubility
Marcos Gil-García, Manuel Bañó‐Polo, Nathalia Varejão, et al.
Molecular Pharmaceutics (2018) Vol. 15, Iss. 9, pp. 3846-3859
Closed Access | Times Cited: 53

Epigenetic silencing by the SMC5/6 complex mediates HIV-1 latency
Ishak D. Irwan, Hal P. Bogerd, Bryan R. Cullen
Nature Microbiology (2022) Vol. 7, Iss. 12, pp. 2101-2113
Open Access | Times Cited: 23

SUMOylation of RNF146 results in Axin degradation and activation of Wnt/β-catenin signaling to promote the progression of hepatocellular carcinoma
Wenjia Li, Qingfang Han, Yuanxin Zhu, et al.
Oncogene (2023) Vol. 42, Iss. 21, pp. 1728-1740
Open Access | Times Cited: 16

A R-loop sensing pathway mediates the relocation of transcribed genes to nuclear pore complexes
Arianna Penzo, Marion Dubarry, Clémentine Brocas, et al.
Nature Communications (2023) Vol. 14, Iss. 1
Open Access | Times Cited: 13

SMC5/6: Multifunctional Player in Replication
Jan Paleček
Genes (2018) Vol. 10, Iss. 1, pp. 7-7
Open Access | Times Cited: 46

SUMO Chains Rule on Chromatin Occupancy
Jan Keiten‐Schmitz, Kathrin Schunck, Stefan Müller
Frontiers in Cell and Developmental Biology (2020) Vol. 7
Open Access | Times Cited: 37

Stabilization of DNA fork junctions by Smc5/6 complexes revealed by single-molecule imaging
Nicoleta-Loredana Tanasie, Pilar Gutiérrez-Escribano, Sigrun Jaklin, et al.
Cell Reports (2022) Vol. 41, Iss. 10, pp. 111778-111778
Open Access | Times Cited: 21

Cryo-EM structure of the Smc5/6 holo-complex
Stephen T. Hallett, Isabella Campbell Harry, Pascale Schellenberger, et al.
Nucleic Acids Research (2022) Vol. 50, Iss. 16, pp. 9505-9520
Open Access | Times Cited: 20

SUMO-activated target traps (SATTs) enable the identification of a comprehensive E3-specific SUMO proteome
Daniel Salas‐Lloret, Nicolette S. Jansen, Easa Nagamalleswari, et al.
Science Advances (2023) Vol. 9, Iss. 31
Open Access | Times Cited: 12

Live-cell single-molecule tracking highlights requirements for stable Smc5/6 chromatin association in vivo
Thomas J. Etheridge, D. Villahermosa, Eduard Campillo-Funollet, et al.
eLife (2021) Vol. 10
Open Access | Times Cited: 25

Structural basis for the E3 ligase activity enhancement of yeast Nse2 by SUMO-interacting motifs
Nathalia Varejão, Jara Lascorz, Joan Codina-Fabra, et al.
Nature Communications (2021) Vol. 12, Iss. 1
Open Access | Times Cited: 24

Smc5/6, an atypical SMC complex with two RING-type subunits
Roger Solé-Soler, Jordi Torres‐Rosell
Biochemical Society Transactions (2020) Vol. 48, Iss. 5, pp. 2159-2171
Closed Access | Times Cited: 24

The Role of SUMO E3 Ligases in Signaling Pathway of Cancer Cells
Xiaoxia Shi, Yixin Du, Shujing Li, et al.
International Journal of Molecular Sciences (2022) Vol. 23, Iss. 7, pp. 3639-3639
Open Access | Times Cited: 16

Brc1 Promotes the Focal Accumulation and SUMO Ligase Activity of Smc5-Smc6 during Replication Stress
Martina Oravcová, Mariana C. Gadaleta, Minghua Nie, et al.
Molecular and Cellular Biology (2018) Vol. 39, Iss. 2
Open Access | Times Cited: 26

Insights into the transcriptional and post-transcriptional regulation of the rice SUMOylation machinery and into the role of two rice SUMO proteases
Margarida T. G. Rosa, Diego M. Almeida, Inês Pires, et al.
BMC Plant Biology (2018) Vol. 18, Iss. 1
Open Access | Times Cited: 25

Hit the brakes – a new perspective on the loop extrusion mechanism of cohesin and other SMC complexes
Avi Matityahu, Itay Onn
Journal of Cell Science (2021) Vol. 134, Iss. 1
Open Access | Times Cited: 19

Plant SUMO E3 Ligases: Function, Structural Organization, and Connection With DNA
Souleimen Jmii, Laurent Cappadocia
Frontiers in Plant Science (2021) Vol. 12
Open Access | Times Cited: 19

Recruitment, loading, and activation of the Smc5–Smc6 SUMO ligase
Martina Oravcová, Michael N. Boddy
Current Genetics (2019) Vol. 65, Iss. 3, pp. 669-676
Open Access | Times Cited: 20

Sumoylation of Smc5 Promotes Error-free Bypass at Damaged Replication Forks
Mariel Zapatka, Irene Pociño-Merino, Hayat Heluani‐Gahete, et al.
Cell Reports (2019) Vol. 29, Iss. 10, pp. 3160-3172.e4
Open Access | Times Cited: 20

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